HEADER LYASE/TRANSFERASE 12-NOV-01 1GPW
TITLE STRUCTURAL EVIDENCE FOR AMMONIA TUNNELING ACROSS THE (BETA/ALPHA)8
TITLE 2 BARREL OF THE IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE BIENZYME COMPLEX.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISF PROTEIN;
COMPND 3 CHAIN: A, C, E;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: AMIDOTRANSFERASE HISH;
COMPND 8 CHAIN: B, D, F;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: W3110;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: W3110 DELTA-TRPEA2;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: RBSIISPHI-THISH;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 11 ORGANISM_TAXID: 2336;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 EXPRESSION_SYSTEM_STRAIN: W3110;
SOURCE 15 EXPRESSION_SYSTEM_VARIANT: W3110 DELTA-TRPEA2;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: RBSIISPHI-THISH
KEYWDS LYASE/TRANSFERASE, COMPLEX (LYASE-TRANSFERASE), HISTIDINE
KEYWDS 2 BIOSYNTHESIS, GLUTAMINASE, GLUTAMINE AMIDOTRANSFERASE, CYCLASE,
KEYWDS 3 AMMONIA CHANNEL, LYASE-TRANSFERASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WALKER,S.BEISMANN-DRIEMEYER,R.STERNER,M.WILMANNS
REVDAT 5 13-DEC-23 1GPW 1 REMARK
REVDAT 4 24-JUL-19 1GPW 1 REMARK
REVDAT 3 12-JUL-17 1GPW 1
REVDAT 2 24-FEB-09 1GPW 1 VERSN
REVDAT 1 10-FEB-02 1GPW 0
JRNL AUTH A.DOUANGAMATH,M.WALKER,S.BEISMANN-DRIEMEYER,
JRNL AUTH 2 M.C.VEGA-FERNANDEZ,R.STERNER,M.WILMANNS
JRNL TITL STRUCTURAL EVIDENCE FOR AMMONIA TUNNELING ACROSS THE (BETA
JRNL TITL 2 ALPHA)(8) BARREL OF THE IMIDAZOLE GLYCEROL PHOSPHATE
JRNL TITL 3 SYNTHASE BIENZYME COMPLEX.
JRNL REF STRUCTURE V. 10 185 2002
JRNL REFN ISSN 0969-2126
JRNL PMID 11839304
JRNL DOI 10.1016/S0969-2126(02)00702-5
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.BEISMANN-DRIEMEYER,R.STERNER
REMARK 1 TITL IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE FROM THERMOTOGA
REMARK 1 TITL 2 MARITIMA
REMARK 1 REF J.BIOL.CHEM. V. 276 20387 2001
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 11264293
REMARK 1 DOI 10.1074/JBC.M102012200
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 65356
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3327
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 9566
REMARK 3 BIN R VALUE (WORKING SET) : 0.3110
REMARK 3 BIN FREE R VALUE : 0.4060
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 529
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10643
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 459
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 46.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 22.48000
REMARK 3 B22 (A**2) : -9.16000
REMARK 3 B33 (A**2) : -13.33000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 7.36000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.33
REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.47
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.47
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.820
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 9.630 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 9.730 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 13.340; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 13.920; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.32
REMARK 3 BSOL : 59.62
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : ION.PARA
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GPW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1290008837.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.88
REMARK 200 MONOCHROMATOR : TRIANGULAR
REMARK 200 OPTICS : BENT MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : X-RAY RESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65356
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.370
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.16800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1THF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 10 MM TRIS (PH 8.0),
REMARK 280 1 MM DTT, 1 MM EDTA, 28.8 MG/ML PROTEIN COMPLEX. PRECIPITATE
REMARK 280 SOLUTION: 15 %[W/V] PEG-8000, 0.9 M AMMONIUM NITRATE, 0.1 M
REMARK 280 HEPES/HCL (PH 8.5), 10 MM DTT, 5% [V/V] MPD, PH 8.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 45.95000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICALLY RELEVANT UNITS ARE THE
REMARK 300 FOLLOWING HETERODIMERS:HISF/HISH CHAIN A/CHAIN B
REMARK 300 , HISF/HISH CHAIN C/CHAIN D, HISF/HISHCHAIN E/
REMARK 300 CHAIN F. THERE ARE SIGNIFICANT CONFORMATIONAL
REMARK 300 DIFFERENCESIN THE THREE HETERO-DIMERS, HENCE THEY
REMARK 300 CANNOT BE RELATED BYUNIQUE SETS OF NCS OPERATORS.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY E 20
REMARK 465 THR E 21
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 24 CG CD OE1 OE2
REMARK 470 ASN A 25 CG OD1 ND2
REMARK 470 LYS A 60 CG CD CE NZ
REMARK 470 LEU A 253 CG CD1 CD2
REMARK 470 ARG B 201 CA C O CB CG CD NE
REMARK 470 ARG B 201 CZ NH1 NH2
REMARK 470 LYS C 19 CG CD CE NZ
REMARK 470 PHE C 23 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU C 24 CG CD OE1 OE2
REMARK 470 ASN D 40 CG OD1 ND2
REMARK 470 ARG D 200 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 201 CG CD NE CZ NH1 NH2
REMARK 470 PHE E 23 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN E 25 CG OD1 ND2
REMARK 470 LYS E 60 CG CD CE NZ
REMARK 470 SER F 199 OG
REMARK 470 ARG F 200 CG CD NE CZ NH1 NH2
REMARK 470 ARG F 201 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ARG D 39 N ASP D 41 2.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 N SER C 55 CB ARG F 200 1456 1.73
REMARK 500 NH2 ARG B 114 OE2 GLU E 208 1455 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO D 98 C - N - CA ANGL. DEV. = 9.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 14 47.87 38.48
REMARK 500 ASN A 22 -175.80 167.93
REMARK 500 GLU A 24 -96.16 -10.02
REMARK 500 ALA A 54 -73.67 -18.95
REMARK 500 SER A 55 -69.22 159.80
REMARK 500 ASN A 103 -78.68 -129.61
REMARK 500 LYS A 179 13.02 58.57
REMARK 500 ALA A 224 -58.43 -125.84
REMARK 500 SER A 225 -77.63 -43.60
REMARK 500 ARG A 230 3.48 83.08
REMARK 500 GLU A 251 -118.91 -64.10
REMARK 500 GLU B 25 -76.43 -50.00
REMARK 500 ASN B 26 52.51 -67.16
REMARK 500 ASP B 29 70.97 13.47
REMARK 500 PRO B 49 -155.55 -81.66
REMARK 500 VAL B 51 113.33 -160.64
REMARK 500 ASP B 65 60.91 35.03
REMARK 500 CYS B 84 -132.88 67.04
REMARK 500 LEU B 85 -36.94 -39.38
REMARK 500 ARG B 114 64.67 -100.03
REMARK 500 ARG B 117 63.29 -102.53
REMARK 500 LEU B 118 -67.02 -26.55
REMARK 500 ASP B 130 179.87 175.63
REMARK 500 THR B 131 -68.27 69.55
REMARK 500 VAL B 140 76.29 -155.46
REMARK 500 SER B 182 32.84 -99.84
REMARK 500 SER B 183 -142.66 52.40
REMARK 500 ARG B 200 -149.21 162.39
REMARK 500 VAL C 18 -155.15 -67.60
REMARK 500 LYS C 19 51.24 146.92
REMARK 500 ASN C 22 76.07 51.59
REMARK 500 ASN C 25 86.78 83.74
REMARK 500 ARG C 27 -124.83 -111.82
REMARK 500 ASP C 28 137.58 177.44
REMARK 500 ALA C 54 179.26 -53.92
REMARK 500 ASN C 103 -81.54 -120.85
REMARK 500 ASN C 109 75.96 -178.75
REMARK 500 ASP C 176 118.27 -36.74
REMARK 500 ALA C 224 -70.30 -133.21
REMARK 500 ARG D 39 44.34 -106.84
REMARK 500 ASN D 40 -30.14 30.45
REMARK 500 PRO D 49 -153.62 -87.66
REMARK 500 CYS D 84 -103.44 53.40
REMARK 500 PRO D 98 -115.72 -6.67
REMARK 500 LEU D 118 -84.14 -16.82
REMARK 500 ASP D 130 -174.58 -174.37
REMARK 500 THR D 131 -63.01 57.92
REMARK 500 VAL D 140 90.52 -162.08
REMARK 500 SER D 183 -140.14 53.53
REMARK 500 SER D 199 -89.50 -69.49
REMARK 500
REMARK 500 THIS ENTRY HAS 102 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 517 DISTANCE = 8.65 ANGSTROMS
REMARK 525 HOH B 349 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH F 371 DISTANCE = 5.86 ANGSTROMS
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "EA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 E 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1THF RELATED DB: PDB
REMARK 900 CYCLASE SUBUNIT OF IMIDAZOLEGLYCEROLPHOSPHATE SYNTHASE FROM
REMARK 900 THERMOTOGA MARITIMA
DBREF 1GPW A 1 253 UNP Q9X0C6 Q9X0C6 1 253
DBREF 1GPW B 1 201 UNP Q9X0C8 HIS5_THEMA 1 201
DBREF 1GPW C 1 253 UNP Q9X0C6 Q9X0C6 1 253
DBREF 1GPW D 1 201 UNP Q9X0C8 HIS5_THEMA 1 201
DBREF 1GPW E 1 253 UNP Q9X0C6 Q9X0C6 1 253
DBREF 1GPW F 1 201 UNP Q9X0C8 HIS5_THEMA 1 201
SEQADV 1GPW ASN A 11 UNP Q9X0C6 ASP 11 ENGINEERED MUTATION
SEQADV 1GPW ASN C 11 UNP Q9X0C6 ASP 11 ENGINEERED MUTATION
SEQADV 1GPW ASN E 11 UNP Q9X0C6 ASP 11 ENGINEERED MUTATION
SEQRES 1 A 253 MET LEU ALA LYS ARG ILE ILE ALA CYS LEU ASN VAL LYS
SEQRES 2 A 253 ASP GLY ARG VAL VAL LYS GLY THR ASN PHE GLU ASN LEU
SEQRES 3 A 253 ARG ASP SER GLY ASP PRO VAL GLU LEU GLY LYS PHE TYR
SEQRES 4 A 253 SER GLU ILE GLY ILE ASP GLU LEU VAL PHE LEU ASP ILE
SEQRES 5 A 253 THR ALA SER VAL GLU LYS ARG LYS THR MET LEU GLU LEU
SEQRES 6 A 253 VAL GLU LYS VAL ALA GLU GLN ILE ASP ILE PRO PHE THR
SEQRES 7 A 253 VAL GLY GLY GLY ILE HIS ASP PHE GLU THR ALA SER GLU
SEQRES 8 A 253 LEU ILE LEU ARG GLY ALA ASP LYS VAL SER ILE ASN THR
SEQRES 9 A 253 ALA ALA VAL GLU ASN PRO SER LEU ILE THR GLN ILE ALA
SEQRES 10 A 253 GLN THR PHE GLY SER GLN ALA VAL VAL VAL ALA ILE ASP
SEQRES 11 A 253 ALA LYS ARG VAL ASP GLY GLU PHE MET VAL PHE THR TYR
SEQRES 12 A 253 SER GLY LYS LYS ASN THR GLY ILE LEU LEU ARG ASP TRP
SEQRES 13 A 253 VAL VAL GLU VAL GLU LYS ARG GLY ALA GLY GLU ILE LEU
SEQRES 14 A 253 LEU THR SER ILE ASP ARG ASP GLY THR LYS SER GLY TYR
SEQRES 15 A 253 ASP THR GLU MET ILE ARG PHE VAL ARG PRO LEU THR THR
SEQRES 16 A 253 LEU PRO ILE ILE ALA SER GLY GLY ALA GLY LYS MET GLU
SEQRES 17 A 253 HIS PHE LEU GLU ALA PHE LEU ALA GLY ALA ASP ALA ALA
SEQRES 18 A 253 LEU ALA ALA SER VAL PHE HIS PHE ARG GLU ILE ASP VAL
SEQRES 19 A 253 ARG GLU LEU LYS GLU TYR LEU LYS LYS HIS GLY VAL ASN
SEQRES 20 A 253 VAL ARG LEU GLU GLY LEU
SEQRES 1 B 201 MET ARG ILE GLY ILE ILE SER VAL GLY PRO GLY ASN ILE
SEQRES 2 B 201 MET ASN LEU TYR ARG GLY VAL LYS ARG ALA SER GLU ASN
SEQRES 3 B 201 PHE GLU ASP VAL SER ILE GLU LEU VAL GLU SER PRO ARG
SEQRES 4 B 201 ASN ASP LEU TYR ASP LEU LEU PHE ILE PRO GLY VAL GLY
SEQRES 5 B 201 HIS PHE GLY GLU GLY MET ARG ARG LEU ARG GLU ASN ASP
SEQRES 6 B 201 LEU ILE ASP PHE VAL ARG LYS HIS VAL GLU ASP GLU ARG
SEQRES 7 B 201 TYR VAL VAL GLY VAL CYS LEU GLY MET GLN LEU LEU PHE
SEQRES 8 B 201 GLU GLU SER GLU GLU ALA PRO GLY VAL LYS GLY LEU SER
SEQRES 9 B 201 LEU ILE GLU GLY ASN VAL VAL LYS LEU ARG SER ARG ARG
SEQRES 10 B 201 LEU PRO HIS MET GLY TRP ASN GLU VAL ILE PHE LYS ASP
SEQRES 11 B 201 THR PHE PRO ASN GLY TYR TYR TYR PHE VAL HIS THR TYR
SEQRES 12 B 201 ARG ALA VAL CYS GLU GLU GLU HIS VAL LEU GLY THR THR
SEQRES 13 B 201 GLU TYR ASP GLY GLU ILE PHE PRO SER ALA VAL ARG LYS
SEQRES 14 B 201 GLY ARG ILE LEU GLY PHE GLN PHE HIS PRO GLU LYS SER
SEQRES 15 B 201 SER LYS ILE GLY ARG LYS LEU LEU GLU LYS VAL ILE GLU
SEQRES 16 B 201 CYS SER LEU SER ARG ARG
SEQRES 1 C 253 MET LEU ALA LYS ARG ILE ILE ALA CYS LEU ASN VAL LYS
SEQRES 2 C 253 ASP GLY ARG VAL VAL LYS GLY THR ASN PHE GLU ASN LEU
SEQRES 3 C 253 ARG ASP SER GLY ASP PRO VAL GLU LEU GLY LYS PHE TYR
SEQRES 4 C 253 SER GLU ILE GLY ILE ASP GLU LEU VAL PHE LEU ASP ILE
SEQRES 5 C 253 THR ALA SER VAL GLU LYS ARG LYS THR MET LEU GLU LEU
SEQRES 6 C 253 VAL GLU LYS VAL ALA GLU GLN ILE ASP ILE PRO PHE THR
SEQRES 7 C 253 VAL GLY GLY GLY ILE HIS ASP PHE GLU THR ALA SER GLU
SEQRES 8 C 253 LEU ILE LEU ARG GLY ALA ASP LYS VAL SER ILE ASN THR
SEQRES 9 C 253 ALA ALA VAL GLU ASN PRO SER LEU ILE THR GLN ILE ALA
SEQRES 10 C 253 GLN THR PHE GLY SER GLN ALA VAL VAL VAL ALA ILE ASP
SEQRES 11 C 253 ALA LYS ARG VAL ASP GLY GLU PHE MET VAL PHE THR TYR
SEQRES 12 C 253 SER GLY LYS LYS ASN THR GLY ILE LEU LEU ARG ASP TRP
SEQRES 13 C 253 VAL VAL GLU VAL GLU LYS ARG GLY ALA GLY GLU ILE LEU
SEQRES 14 C 253 LEU THR SER ILE ASP ARG ASP GLY THR LYS SER GLY TYR
SEQRES 15 C 253 ASP THR GLU MET ILE ARG PHE VAL ARG PRO LEU THR THR
SEQRES 16 C 253 LEU PRO ILE ILE ALA SER GLY GLY ALA GLY LYS MET GLU
SEQRES 17 C 253 HIS PHE LEU GLU ALA PHE LEU ALA GLY ALA ASP ALA ALA
SEQRES 18 C 253 LEU ALA ALA SER VAL PHE HIS PHE ARG GLU ILE ASP VAL
SEQRES 19 C 253 ARG GLU LEU LYS GLU TYR LEU LYS LYS HIS GLY VAL ASN
SEQRES 20 C 253 VAL ARG LEU GLU GLY LEU
SEQRES 1 D 201 MET ARG ILE GLY ILE ILE SER VAL GLY PRO GLY ASN ILE
SEQRES 2 D 201 MET ASN LEU TYR ARG GLY VAL LYS ARG ALA SER GLU ASN
SEQRES 3 D 201 PHE GLU ASP VAL SER ILE GLU LEU VAL GLU SER PRO ARG
SEQRES 4 D 201 ASN ASP LEU TYR ASP LEU LEU PHE ILE PRO GLY VAL GLY
SEQRES 5 D 201 HIS PHE GLY GLU GLY MET ARG ARG LEU ARG GLU ASN ASP
SEQRES 6 D 201 LEU ILE ASP PHE VAL ARG LYS HIS VAL GLU ASP GLU ARG
SEQRES 7 D 201 TYR VAL VAL GLY VAL CYS LEU GLY MET GLN LEU LEU PHE
SEQRES 8 D 201 GLU GLU SER GLU GLU ALA PRO GLY VAL LYS GLY LEU SER
SEQRES 9 D 201 LEU ILE GLU GLY ASN VAL VAL LYS LEU ARG SER ARG ARG
SEQRES 10 D 201 LEU PRO HIS MET GLY TRP ASN GLU VAL ILE PHE LYS ASP
SEQRES 11 D 201 THR PHE PRO ASN GLY TYR TYR TYR PHE VAL HIS THR TYR
SEQRES 12 D 201 ARG ALA VAL CYS GLU GLU GLU HIS VAL LEU GLY THR THR
SEQRES 13 D 201 GLU TYR ASP GLY GLU ILE PHE PRO SER ALA VAL ARG LYS
SEQRES 14 D 201 GLY ARG ILE LEU GLY PHE GLN PHE HIS PRO GLU LYS SER
SEQRES 15 D 201 SER LYS ILE GLY ARG LYS LEU LEU GLU LYS VAL ILE GLU
SEQRES 16 D 201 CYS SER LEU SER ARG ARG
SEQRES 1 E 253 MET LEU ALA LYS ARG ILE ILE ALA CYS LEU ASN VAL LYS
SEQRES 2 E 253 ASP GLY ARG VAL VAL LYS GLY THR ASN PHE GLU ASN LEU
SEQRES 3 E 253 ARG ASP SER GLY ASP PRO VAL GLU LEU GLY LYS PHE TYR
SEQRES 4 E 253 SER GLU ILE GLY ILE ASP GLU LEU VAL PHE LEU ASP ILE
SEQRES 5 E 253 THR ALA SER VAL GLU LYS ARG LYS THR MET LEU GLU LEU
SEQRES 6 E 253 VAL GLU LYS VAL ALA GLU GLN ILE ASP ILE PRO PHE THR
SEQRES 7 E 253 VAL GLY GLY GLY ILE HIS ASP PHE GLU THR ALA SER GLU
SEQRES 8 E 253 LEU ILE LEU ARG GLY ALA ASP LYS VAL SER ILE ASN THR
SEQRES 9 E 253 ALA ALA VAL GLU ASN PRO SER LEU ILE THR GLN ILE ALA
SEQRES 10 E 253 GLN THR PHE GLY SER GLN ALA VAL VAL VAL ALA ILE ASP
SEQRES 11 E 253 ALA LYS ARG VAL ASP GLY GLU PHE MET VAL PHE THR TYR
SEQRES 12 E 253 SER GLY LYS LYS ASN THR GLY ILE LEU LEU ARG ASP TRP
SEQRES 13 E 253 VAL VAL GLU VAL GLU LYS ARG GLY ALA GLY GLU ILE LEU
SEQRES 14 E 253 LEU THR SER ILE ASP ARG ASP GLY THR LYS SER GLY TYR
SEQRES 15 E 253 ASP THR GLU MET ILE ARG PHE VAL ARG PRO LEU THR THR
SEQRES 16 E 253 LEU PRO ILE ILE ALA SER GLY GLY ALA GLY LYS MET GLU
SEQRES 17 E 253 HIS PHE LEU GLU ALA PHE LEU ALA GLY ALA ASP ALA ALA
SEQRES 18 E 253 LEU ALA ALA SER VAL PHE HIS PHE ARG GLU ILE ASP VAL
SEQRES 19 E 253 ARG GLU LEU LYS GLU TYR LEU LYS LYS HIS GLY VAL ASN
SEQRES 20 E 253 VAL ARG LEU GLU GLY LEU
SEQRES 1 F 201 MET ARG ILE GLY ILE ILE SER VAL GLY PRO GLY ASN ILE
SEQRES 2 F 201 MET ASN LEU TYR ARG GLY VAL LYS ARG ALA SER GLU ASN
SEQRES 3 F 201 PHE GLU ASP VAL SER ILE GLU LEU VAL GLU SER PRO ARG
SEQRES 4 F 201 ASN ASP LEU TYR ASP LEU LEU PHE ILE PRO GLY VAL GLY
SEQRES 5 F 201 HIS PHE GLY GLU GLY MET ARG ARG LEU ARG GLU ASN ASP
SEQRES 6 F 201 LEU ILE ASP PHE VAL ARG LYS HIS VAL GLU ASP GLU ARG
SEQRES 7 F 201 TYR VAL VAL GLY VAL CYS LEU GLY MET GLN LEU LEU PHE
SEQRES 8 F 201 GLU GLU SER GLU GLU ALA PRO GLY VAL LYS GLY LEU SER
SEQRES 9 F 201 LEU ILE GLU GLY ASN VAL VAL LYS LEU ARG SER ARG ARG
SEQRES 10 F 201 LEU PRO HIS MET GLY TRP ASN GLU VAL ILE PHE LYS ASP
SEQRES 11 F 201 THR PHE PRO ASN GLY TYR TYR TYR PHE VAL HIS THR TYR
SEQRES 12 F 201 ARG ALA VAL CYS GLU GLU GLU HIS VAL LEU GLY THR THR
SEQRES 13 F 201 GLU TYR ASP GLY GLU ILE PHE PRO SER ALA VAL ARG LYS
SEQRES 14 F 201 GLY ARG ILE LEU GLY PHE GLN PHE HIS PRO GLU LYS SER
SEQRES 15 F 201 SER LYS ILE GLY ARG LYS LEU LEU GLU LYS VAL ILE GLU
SEQRES 16 F 201 CYS SER LEU SER ARG ARG
HET PO4 A 301 5
HET PO4 A 302 5
HET PO4 C 301 5
HET PO4 C 302 5
HET PO4 C 303 5
HET PO4 E 301 5
HETNAM PO4 PHOSPHATE ION
FORMUL 7 PO4 6(O4 P 3-)
FORMUL 13 HOH *459(H2 O)
HELIX 1 AA1 ASP A 31 GLY A 43 1 13
HELIX 2 AA2 GLU A 57 GLU A 71 1 15
HELIX 3 AA3 ASP A 85 GLY A 96 1 12
HELIX 4 AA4 ASN A 103 ASN A 109 1 7
HELIX 5 AA5 PRO A 110 GLY A 121 1 12
HELIX 6 AA6 LEU A 153 GLY A 164 1 12
HELIX 7 AA7 ASP A 183 ARG A 191 1 9
HELIX 8 AA8 PRO A 192 THR A 194 5 3
HELIX 9 AA9 LYS A 206 ALA A 216 1 11
HELIX 10 AB1 ALA A 224 PHE A 229 1 6
HELIX 11 AB2 ASP A 233 HIS A 244 1 12
HELIX 12 AB3 ILE B 13 SER B 24 1 12
HELIX 13 AB4 PHE B 54 ASN B 64 1 11
HELIX 14 AB5 LEU B 66 ASP B 76 1 11
HELIX 15 AB6 CYS B 84 LEU B 89 1 6
HELIX 16 AB7 HIS B 178 LYS B 181 5 4
HELIX 17 AB8 SER B 182 SER B 197 1 16
HELIX 18 AB9 ASP C 31 GLY C 43 1 13
HELIX 19 AC1 GLU C 57 GLU C 71 1 15
HELIX 20 AC2 ASP C 85 ARG C 95 1 11
HELIX 21 AC3 ASN C 103 GLU C 108 1 6
HELIX 22 AC4 PRO C 110 GLY C 121 1 12
HELIX 23 AC5 LEU C 153 ARG C 163 1 11
HELIX 24 AC6 ASP C 183 ARG C 191 1 9
HELIX 25 AC7 PRO C 192 THR C 194 5 3
HELIX 26 AC8 LYS C 206 ALA C 216 1 11
HELIX 27 AC9 ALA C 224 PHE C 229 1 6
HELIX 28 AD1 ASP C 233 HIS C 244 1 12
HELIX 29 AD2 ILE D 13 GLU D 25 1 13
HELIX 30 AD3 PHE D 54 ASN D 64 1 11
HELIX 31 AD4 LEU D 66 ASP D 76 1 11
HELIX 32 AD5 CYS D 84 LEU D 89 1 6
HELIX 33 AD6 GLU D 148 GLU D 150 5 3
HELIX 34 AD7 HIS D 178 LYS D 181 5 4
HELIX 35 AD8 SER D 182 SER D 197 1 16
HELIX 36 AD9 ASP E 31 GLY E 43 1 13
HELIX 37 AE1 GLU E 57 GLU E 71 1 15
HELIX 38 AE2 ASP E 85 GLY E 96 1 12
HELIX 39 AE3 ASN E 103 ASN E 109 1 7
HELIX 40 AE4 PRO E 110 GLY E 121 1 12
HELIX 41 AE5 ARG E 133 GLU E 137 5 5
HELIX 42 AE6 TYR E 143 LYS E 146 5 4
HELIX 43 AE7 LEU E 153 GLY E 164 1 12
HELIX 44 AE8 ASP E 183 ARG E 191 1 9
HELIX 45 AE9 PRO E 192 THR E 194 5 3
HELIX 46 AF1 LYS E 206 ALA E 216 1 11
HELIX 47 AF2 ALA E 224 ARG E 230 1 7
HELIX 48 AF3 ASP E 233 LYS E 243 1 11
HELIX 49 AF4 ILE F 13 GLU F 25 1 13
HELIX 50 AF5 PHE F 54 GLU F 63 1 10
HELIX 51 AF6 LEU F 66 ASP F 76 1 11
HELIX 52 AF7 CYS F 84 LEU F 89 1 6
HELIX 53 AF8 HIS F 178 LYS F 181 5 4
HELIX 54 AF9 SER F 182 SER F 197 1 16
SHEET 1 AA1 9 ARG A 27 ASP A 28 0
SHEET 2 AA1 9 ARG A 16 LYS A 19 -1 N LYS A 19 O ARG A 27
SHEET 3 AA1 9 ARG A 5 LYS A 13 -1 N LYS A 13 O ARG A 16
SHEET 4 AA1 9 GLU A 46 ASP A 51 1 O VAL A 48 N LEU A 10
SHEET 5 AA1 9 PHE A 77 GLY A 80 1 O THR A 78 N LEU A 47
SHEET 6 AA1 9 LYS A 99 ILE A 102 1 O SER A 101 N VAL A 79
SHEET 7 AA1 9 VAL A 125 VAL A 134 1 O VAL A 126 N VAL A 100
SHEET 8 AA1 9 GLU A 137 THR A 142 -1 O GLU A 137 N VAL A 134
SHEET 9 AA1 9 LYS A 147 LEU A 152 -1 O ILE A 151 N VAL A 140
SHEET 1 AA2 9 ARG A 27 ASP A 28 0
SHEET 2 AA2 9 ARG A 16 LYS A 19 -1 N LYS A 19 O ARG A 27
SHEET 3 AA2 9 ARG A 5 LYS A 13 -1 N LYS A 13 O ARG A 16
SHEET 4 AA2 9 ALA A 220 ALA A 223 1 O ALA A 221 N ILE A 7
SHEET 5 AA2 9 ILE A 198 SER A 201 1 N ALA A 200 O ALA A 220
SHEET 6 AA2 9 GLU A 167 SER A 172 1 N ILE A 168 O ILE A 199
SHEET 7 AA2 9 VAL A 125 VAL A 134 1 N ILE A 129 O LEU A 169
SHEET 8 AA2 9 GLU A 137 THR A 142 -1 O GLU A 137 N VAL A 134
SHEET 9 AA2 9 LYS A 147 LEU A 152 -1 O ILE A 151 N VAL A 140
SHEET 1 AA3 9 SER B 31 VAL B 35 0
SHEET 2 AA3 9 ARG B 2 ILE B 6 1 N ILE B 5 O GLU B 33
SHEET 3 AA3 9 LEU B 45 ILE B 48 1 O LEU B 45 N GLY B 4
SHEET 4 AA3 9 TYR B 79 VAL B 83 1 O VAL B 81 N LEU B 46
SHEET 5 AA3 9 ILE B 172 PHE B 175 1 O LEU B 173 N GLY B 82
SHEET 6 AA3 9 GLU B 161 LYS B 169 -1 N VAL B 167 O GLY B 174
SHEET 7 AA3 9 VAL B 152 TYR B 158 -1 N TYR B 158 O GLU B 161
SHEET 8 AA3 9 HIS B 120 PHE B 128 -1 N ILE B 127 O THR B 155
SHEET 9 AA3 9 GLY B 135 HIS B 141 -1 O GLY B 135 N VAL B 126
SHEET 1 AA4 2 GLU B 93 SER B 94 0
SHEET 2 AA4 2 ALA B 97 LYS B 101 -1 O ALA B 97 N SER B 94
SHEET 1 AA5 2 GLY B 108 LYS B 112 0
SHEET 2 AA5 2 TYR B 143 CYS B 147 -1 O ARG B 144 N VAL B 111
SHEET 1 AA6 8 ARG C 16 VAL C 17 0
SHEET 2 AA6 8 ARG C 5 LYS C 13 -1 N LYS C 13 O ARG C 16
SHEET 3 AA6 8 GLU C 46 ASP C 51 1 O LEU C 50 N VAL C 12
SHEET 4 AA6 8 PHE C 77 GLY C 80 1 O THR C 78 N PHE C 49
SHEET 5 AA6 8 LYS C 99 ILE C 102 1 O SER C 101 N VAL C 79
SHEET 6 AA6 8 VAL C 125 VAL C 134 1 O VAL C 126 N VAL C 100
SHEET 7 AA6 8 GLU C 137 THR C 142 -1 O GLU C 137 N VAL C 134
SHEET 8 AA6 8 LYS C 147 LEU C 152 -1 O ILE C 151 N VAL C 140
SHEET 1 AA7 8 ARG C 16 VAL C 17 0
SHEET 2 AA7 8 ARG C 5 LYS C 13 -1 N LYS C 13 O ARG C 16
SHEET 3 AA7 8 ALA C 220 ALA C 223 1 O ALA C 223 N CYS C 9
SHEET 4 AA7 8 ILE C 198 SER C 201 1 N ALA C 200 O LEU C 222
SHEET 5 AA7 8 GLU C 167 SER C 172 1 N ILE C 168 O ILE C 199
SHEET 6 AA7 8 VAL C 125 VAL C 134 1 N ILE C 129 O LEU C 169
SHEET 7 AA7 8 GLU C 137 THR C 142 -1 O GLU C 137 N VAL C 134
SHEET 8 AA7 8 LYS C 147 LEU C 152 -1 O ILE C 151 N VAL C 140
SHEET 1 AA8 9 SER D 31 VAL D 35 0
SHEET 2 AA8 9 ARG D 2 ILE D 6 1 N ILE D 3 O SER D 31
SHEET 3 AA8 9 LEU D 45 ILE D 48 1 O LEU D 45 N GLY D 4
SHEET 4 AA8 9 TYR D 79 VAL D 83 1 O VAL D 81 N ILE D 48
SHEET 5 AA8 9 ILE D 172 PHE D 175 1 O LEU D 173 N VAL D 80
SHEET 6 AA8 9 GLU D 161 LYS D 169 -1 N VAL D 167 O GLY D 174
SHEET 7 AA8 9 VAL D 152 TYR D 158 -1 N THR D 156 O PHE D 163
SHEET 8 AA8 9 HIS D 120 PHE D 128 -1 N ILE D 127 O THR D 155
SHEET 9 AA8 9 GLY D 135 HIS D 141 -1 O PHE D 139 N GLY D 122
SHEET 1 AA9 2 ASN D 109 LYS D 112 0
SHEET 2 AA9 2 TYR D 143 VAL D 146 -1 O ARG D 144 N VAL D 111
SHEET 1 AB111 ASN E 148 LEU E 152 0
SHEET 2 AB111 MET E 139 PHE E 141 -1 N VAL E 140 O ILE E 151
SHEET 3 AB111 VAL E 125 LYS E 132 -1 N ASP E 130 O PHE E 141
SHEET 4 AB111 GLU E 167 SER E 172 1 O LEU E 169 N ILE E 129
SHEET 5 AB111 ILE E 198 SER E 201 1 O SER E 201 N LEU E 170
SHEET 6 AB111 ALA E 220 ALA E 223 1 O LEU E 222 N ALA E 200
SHEET 7 AB111 ARG E 5 ASN E 11 1 N ARG E 5 O ALA E 221
SHEET 8 AB111 GLU E 46 LEU E 50 1 O VAL E 48 N LEU E 10
SHEET 9 AB111 PHE E 77 GLY E 80 1 O THR E 78 N LEU E 47
SHEET 10 AB111 LYS E 99 ILE E 102 1 O SER E 101 N VAL E 79
SHEET 11 AB111 VAL E 125 LYS E 132 1 O VAL E 126 N VAL E 100
SHEET 1 AB2 9 SER F 31 VAL F 35 0
SHEET 2 AB2 9 ARG F 2 ILE F 6 1 N ILE F 3 O SER F 31
SHEET 3 AB2 9 LEU F 45 ILE F 48 1 O LEU F 45 N GLY F 4
SHEET 4 AB2 9 TYR F 79 VAL F 83 1 O TYR F 79 N LEU F 46
SHEET 5 AB2 9 ILE F 172 PHE F 175 1 O LEU F 173 N VAL F 80
SHEET 6 AB2 9 GLU F 161 LYS F 169 -1 N LYS F 169 O ILE F 172
SHEET 7 AB2 9 VAL F 152 TYR F 158 -1 N LEU F 153 O ALA F 166
SHEET 8 AB2 9 HIS F 120 PHE F 128 -1 N ILE F 127 O THR F 155
SHEET 9 AB2 9 GLY F 135 HIS F 141 -1 O PHE F 139 N GLY F 122
SHEET 1 AB3 4 ALA F 97 LYS F 101 0
SHEET 2 AB3 4 PHE F 91 SER F 94 -1 N SER F 94 O ALA F 97
SHEET 3 AB3 4 ILE F 106 LYS F 112 1 O VAL F 110 N GLU F 93
SHEET 4 AB3 4 TYR F 143 VAL F 146 -1 O ARG F 144 N VAL F 111
SITE 1 AC1 6 GLY A 81 GLY A 82 HIS A 84 ASN A 103
SITE 2 AC1 6 THR A 104 HOH A 425
SITE 1 AC2 6 ASP A 176 GLY A 177 GLY A 203 ALA A 223
SITE 2 AC2 6 ALA A 224 HOH A 421
SITE 1 AC3 7 ASP C 176 GLY C 177 GLY C 203 ALA C 224
SITE 2 AC3 7 SER C 225 HOH C 411 HOH C 452
SITE 1 AC4 4 GLY C 82 ASN C 103 THR C 104 HOH C 418
SITE 1 AC5 3 LYS C 37 GLN C 72 ASP C 74
SITE 1 AC6 3 GLY E 81 GLY E 82 THR E 104
CRYST1 74.000 91.900 131.000 90.00 105.90 90.00 P 1 21 1 6
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013513 0.000000 0.003849 0.00000
SCALE2 0.000000 0.010881 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007937 0.00000
(ATOM LINES ARE NOT SHOWN.)
END